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P22534

- GUNA_CALSA

UniProt

P22534 - GUNA_CALSA

Protein

Endoglucanase A

Gene

celA

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    • Comment

    Functioni

    The N-terminal domain of CelA codes for an endoglucanase activity on carboxymethylcellulose. The C-terminal domain probably acts synergistically to hydrolyze crystalline cellulose.

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei396 – 3961By similarity
    Active sitei434 – 4341By similarity
    Active sitei443 – 4431By similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. cellulose binding Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiCBM3. Carbohydrate-Binding Module Family 3.
    GH48. Glycoside Hydrolase Family 48.
    GH9. Glycoside Hydrolase Family 9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase A (EC:3.2.1.4)
    Alternative name(s):
    Cellulase A
    Endo-1,4-beta-glucanase A
    Gene namesi
    Name:celA
    OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
    Taxonomic identifieri44001 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 17421719Endoglucanase APRO_0000007944Add
    BLAST

    Post-translational modificationi

    The linker region (also termed "hinge") may be a potential site for proteolysis.

    Structurei

    3D structure databases

    ProteinModelPortaliP22534.
    SMRiP22534. Positions 26-636, 1117-1739.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini477 – 637161CBM3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini703 – 856154CBM3 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini906 – 1059154CBM3 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 476453Catalytic 1Add
    BLAST
    Regioni638 – 70265Linker ("hinge") (Pro-Thr box)Add
    BLAST
    Regioni857 – 90549Linker ("hinge") (Pro-Thr box)Add
    BLAST
    Regioni1060 – 111253Linker ("hinge") (Pro-Thr box)Add
    BLAST
    Regioni1113 – 1742630Catalytic 2Add
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the glycosyl hydrolase 9 (cellulase E) family.Curated
    In the C-terminal section; belongs to the glycosyl hydrolase 48 (cellulase L) family.Curated
    Contains 3 CBM3 (carbohydrate binding type-3) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di1.50.10.10. 5 hits.
    2.60.40.710. 3 hits.
    4.10.870.10. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR027390. Endoglucanase_F_dom3.
    IPR000556. Glyco_hydro_48F.
    IPR001701. Glyco_hydro_9.
    IPR018221. Glyco_hydro_9_AS.
    [Graphical view]
    PfamiPF00942. CBM_3. 3 hits.
    PF02011. Glyco_hydro_48. 1 hit.
    PF00759. Glyco_hydro_9. 1 hit.
    [Graphical view]
    PRINTSiPR00844. GLHYDRLASE48.
    SMARTiSM01067. CBM_3. 3 hits.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 2 hits.
    SSF49384. SSF49384. 3 hits.
    PROSITEiPS51172. CBM3. 3 hits.
    PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
    PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P22534-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVTFLFILG VVYGVKPWQE ARAGSFNYGE ALQKAIMFYE FQMSGKLPNW     50
    VRNNWRGDSA LKDGQDNGLD LTGGWFDAGD HVKFNLPMSY TGTMLSWAAY 100
    EYKDAFVKSG QLEHILNQIE WVNDYFVKCH PSKYVYYYQV GDGGKDHAWW 150
    GPAEVMQMER PSFKVTQSSP GSAVVAETAA SLAAASIVLK DRNPTKAATY 200
    LQHAKDLYEF AEVTKSDSGY TAANGYYNSW SGFYDELSWA AVWLYLATND 250
    STYLTKAESY VQNWPKISGS NIIDYKWAHC WDDVHNGAAL LLAKITDKDT 300
    YKQIIESHLD YWTTGYNGER IKYTPKGLAW LDQWGSLRYA TTTAFLAFVY 350
    SDWSGCPTGK KETYRKFGES QIDYALGSTG RSFVVGFGTN PPKRPHHRTA 400
    HSSWADSQSI PSYHRHTLYG ALVGGPGSDD SYTDDISNYV NNEVACDYNA 450
    GFVGALAKMY LLYGGNPIPD FKAIETPTND EFFVEAGINA SGTNFIEIKA 500
    IVNNQSGWPA RATNKLKFRY FVDLSELIKA GYSPNQLTLS TNYNQGAKVS 550
    GPYVWDSSRN IYYILVDFTG TLIYPGGQDK YKKEVQFRIA APQNVQWDNS 600
    NDYSFQDIKG VSSGSVVKTK YIPLYDEDIK VWGEEPGTSG VSPTPTASVT 650
    PTPTPTPTAT PTPTPTPTVT PTPTVTATPT PTPTPTSTPT VTPTPTPVST 700
    PATSGQIKVL YANKETNSTT NTIRPWLKVV NSGSSSIDLS RVTIRYWYTV 750
    DGERAQSAIS DWAQIGASNV TFKFVKLSSS VSGADYYLEI GFKSGAGQLQ 800
    PGKDTGEIQI RFNKDDWSNY NQGNDWSWIQ SMTSYGENEK VTAYIDGVLV 850
    WGQEPSGTTP APTSTPTVTV TPTPTPTPTV TPTPTVTATP TPTPTPTSTP 900
    VSTPATGGQI KVLYANKETN STTNTIRPWL KVVNSGSSSI DLSRVTIRYW 950
    YTVDGERAQS AISDWAQIGA SNVTFKFVKL SSSVSGADYY LEIGFKSGAG 1000
    QLQPGKDTGE IQIRFNKDDW SNYNQGNDWS WIQSMTSYGE NEKVTAYIDG 1050
    VLVWGQEPSG ATPAPTVTPT PTVTPTPTPA PTPTATPTPT PTPTVTPTPT 1100
    VAPTPTPSST PSGLGKYGQR FMWLWNKIHD PASGYFNQDG IPYHSVETLI 1150
    CEAPDYGHLT TSEAFSYYVW LEAVYGKLTG DWSKFKTAWD TLEKYMIPSA 1200
    EDQPMRSYDP NKPATYAGEW ETPDKYPSPL EFNVPVGKDP LHNELVSTYG 1250
    STLMYGMHWL MDVDNWYGYG KRGDGVSRAS FINTFQRGPE ESVWETVPHP 1300
    SWEEFKWGGP NGFLDLFIKD QNYSKQWRYT NAPDADARAI QATYWAKVWA 1350
    KEQGKFNEIS SYVGKAAKMG DYLRYAMFDK YFKPLGCQDK NAAGGTGYDS 1400
    AHYLLSWYYA WGGALDGAWS WKIGCSHAHF GYQNPMAAWA LANDSDMKPK 1450
    SPNGASDWAK SLKRQIEFYR WLQSAEGAIA GGATNSWNGR YEKYPAGTAT 1500
    FYGMAYEPNP VYRDPGSNTW FGFQAWSMQR VAEYYYVTGD KDAGTLLEKW 1550
    VSWIKSVVKL NSDGTFAIPS TLDWSGQPDT WNGTYTGNPN LHVKVVDYGT 1600
    DLGITASLAN ALLYYSAGTK KYGVFDEEAK NLAKELLDRM WKLYRDEKGL 1650
    SAPEKRADYK RFFEQEVYIP AGWTGKMPNG DVIKSGVKFI DIRSKYKQDP 1700
    DWPKLEAAYK SGQVPEFRYH RFWAQCDIAI VNATYEILFG NQ 1742
    Length:1,742
    Mass (Da):193,697
    Last modified:October 1, 1996 - v2
    Checksum:i3F0699A2123EED07
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1545 – 15451T → A in AAA72860. (PubMed:2039230)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L32742 Genomic DNA. Translation: AAA91086.1.
    M36063 Genomic DNA. Translation: AAA72860.1.
    L01257 Unassigned DNA. No translation available.
    PIRiT17120.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L32742 Genomic DNA. Translation: AAA91086.1 .
    M36063 Genomic DNA. Translation: AAA72860.1 .
    L01257 Unassigned DNA. No translation available.
    PIRi T17120.

    3D structure databases

    ProteinModelPortali P22534.
    SMRi P22534. Positions 26-636, 1117-1739.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM3. Carbohydrate-Binding Module Family 3.
    GH48. Glycoside Hydrolase Family 48.
    GH9. Glycoside Hydrolase Family 9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.50.10.10. 5 hits.
    2.60.40.710. 3 hits.
    4.10.870.10. 1 hit.
    InterProi IPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR027390. Endoglucanase_F_dom3.
    IPR000556. Glyco_hydro_48F.
    IPR001701. Glyco_hydro_9.
    IPR018221. Glyco_hydro_9_AS.
    [Graphical view ]
    Pfami PF00942. CBM_3. 3 hits.
    PF02011. Glyco_hydro_48. 1 hit.
    PF00759. Glyco_hydro_9. 1 hit.
    [Graphical view ]
    PRINTSi PR00844. GLHYDRLASE48.
    SMARTi SM01067. CBM_3. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48208. SSF48208. 2 hits.
    SSF49384. SSF49384. 3 hits.
    PROSITEi PS51172. CBM3. 3 hits.
    PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
    PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "celA, another gene coding for a multidomain cellulase from the extreme thermophile Caldocellum saccharolyticum."
      Te'O V.S. Jr., Saul D.J., Bergquist P.L.
      Appl. Microbiol. Biotechnol. 43:291-296(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for a beta-mannanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum'."
      Luethi E., Jasmat N.B., Grayling R.A., Love D.R., Bergquist P.L.
      Appl. Environ. Microbiol. 57:694-700(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1516-1742.

    Entry informationi

    Entry nameiGUNA_CALSA
    AccessioniPrimary (citable) accession number: P22534
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3